Recombinant human METTL21A protein is typically expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The protein is often fused to a His-tag at the N-terminus to facilitate purification. The recombinant protein is a fragment that spans amino acids 93 to 218, with a molecular weight of approximately 17 kDa .
METTL21A functions as a protein-lysine methyltransferase that selectively trimethylates lysine residues in HSP70 family members . This methylation process is crucial for the regulation of protein function and stability. Specifically, METTL21A contributes to the in vivo trimethylation of lysine residues in several HSP70 proteins, including HSPA1, HSPA2, HSPA5, HSPA6, and HSPA8 . The methylation of these lysine residues can affect the chaperone activity of HSP70 proteins, which are essential for protein folding and protection against stress-induced damage.
The methylation activity of METTL21A has significant implications for cellular processes, particularly in response to stress. By modifying HSP70 proteins, METTL21A helps regulate their function and stability, thereby contributing to the cellular stress response. This regulation is vital for maintaining protein homeostasis and preventing the aggregation of misfolded proteins, which can lead to various diseases .
Recombinant human METTL21A protein is widely used in research to study its enzymatic activity, substrate specificity, and role in cellular processes. It is also utilized in high-throughput screening assays to identify potential inhibitors or modulators of METTL21A activity . The protein’s high purity and specific activity make it suitable for various biochemical and biophysical studies, including SDS-PAGE and mass spectrometry .
Recombinant human METTL21A protein is typically stored in a buffer containing Tris-HCl, sodium chloride, and glycerol to maintain its stability . It can be stored at +2°C to +8°C for short-term use, but for long-term storage, it is recommended to aliquot and store the protein at -20°C to -80°C to avoid repeated freeze-thaw cycles .